View source for 5aq5


==Structure of the Carboxy-Terminal Domain of the Bacteriophage T5 L- Shaped Tail Fibre==
<StructureSection load='5aq5' size='340' side='right'caption='[[5aq5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5aq5]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T5 Escherichia virus T5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AQ5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aq5 OCA], [https://pdbe.org/5aq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aq5 RCSB], [https://www.ebi.ac.uk/pdbsum/5aq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aq5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FIBL1_BPT5 FIBL1_BPT5] Assembles together with p132 to form the three L-shaped long tail fibers and the collar structure at the junction between the tail tube and the conical tail tip (PubMed:24198424). The three L-shaped long tail fibers recognize the host lipopolysaccharides that serve as adhesion receptor for virus entry (PubMed:7045389). Each fiber consists of a thin proximal rod of about 30 nm connected by a hinge to a thicker distal part of about 47 nm (PubMed:24198424).<ref>PMID:24198424</ref> <ref>PMID:7045389</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970-1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 A resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 A structure solved by molecular replacement. The additional chaperone domain (residues 1263-1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition.

Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone.,Garcia-Doval C, Caston JR, Luque D, Granell M, Otero JM, Llamas-Saiz AL, Renouard M, Boulanger P, van Raaij MJ Viruses. 2015 Dec 8;7(12):6424-40. doi: 10.3390/v7122946. PMID:26670244<ref>PMID:26670244</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5aq5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus T5]]
[[Category: Large Structures]]
[[Category: Garcia-Doval C]]
[[Category: Granell M]]
[[Category: Van Raaij MJ]]